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9KZ6

The cryo-EM structure of porcine serum MGAM

Summary for 9KZ6
Entry DOI10.2210/pdb9kz6/pdb
EMDB information62652
DescriptorMaltase-glucoamylase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsalpha-glucosidase, hydrolase
Biological sourceSus scrofa domesticus (domestic pig)
Total number of polymer chains1
Total formula weight208545.49
Authors
Tagami, T.,Kawasaki, M.,Adachi, N. (deposition date: 2024-12-10, release date: 2025-12-10, Last modification date: 2026-01-28)
Primary citationWatanabe, K.,Tagami, T.,Biwa, C.,Kawasaki, M.,Adachi, N.,Moriya, T.,Senda, T.,Okuyama, M.
Porcine serum maltase-glucoamylase: structure, kinetics, and inhibition.
J Enzyme Inhib Med Chem, 41:2612391-2612391, 2026
Cited by
PubMed Abstract: Maltase-glucoamylase (MGAM) is a small-intestinal enzyme comprising two tandem α-glucosidase units, NtMGAM and CtMGAM, each capable of hydrolysing maltodextrins into glucose. MGAM serves as a therapeutic target for managing postprandial hyperglycaemia; comprehensive insights into its full-length three-dimensional structure and inhibitor kinetics remains limited. Here, we demonstrate that the α-glucosidase in porcine serum is comparable to that encoded by the MGAM gene. Using cryo-electron microscopy, we determined the complex structure of serum MGAM with the inhibitor acarviosyl-maltotriose (AC5), which was found to bind exclusively to the active sites of each unit, confirming the presence of independent catalytic sites. AC5 was shown to exhibit mixed-type inhibition towards full-length serum MGAM and competitive inhibition against both recombinant NtMGAM and CtMGAM. The apparent mixed-type inhibition can be more accurately attributed to dual competitive inhibition mechanisms. These findings contribute to the advancement of functional foods and therapeutic interventions for postprandial hyperglycaemia and type 2 diabetes.
PubMed: 41534875
DOI: 10.1080/14756366.2025.2612391
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.17 Å)
Structure validation

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